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Database: PDB
Entry: 4U7T
LinkDB: 4U7T
Original site: 4U7T 
HEADER    TRANSFERASE/TRANSFERASE REGULATOR       31-JUL-14   4U7T              
TITLE     CRYSTAL STRUCTURE OF DNMT3A-DNMT3L IN COMPLEX WITH HISTONE H3         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3A;                     
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 476-912;                                      
COMPND   5 SYNONYM: DNA METHYLTRANSFERASES DNMT3A;                              
COMPND   6 EC: 2.1.1.37;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: DNA (CYTOSINE-5)-METHYLTRANSFERASE 3-LIKE;                 
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: UNP RESIDUES 178-379;                                      
COMPND  12 SYNONYM: DNA METHYLTRANSFERASES DNMT3L;                              
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: PEPTIDE FROM HISTONE H3.3;                                 
COMPND  16 CHAIN: F, G;                                                         
COMPND  17 SYNONYM: HISTONE H3 PEPTIDE;                                         
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DNMT3A;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: DNMT3L;                                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 SYNTHETIC: YES;                                                      
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606                                                 
KEYWDS    DNA METHYLTRANSFERASE, ACTIVE FORM, TRANSFERASE-TRANSFERASE REGULATOR 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.GUO,L.WANG,X.YIN,J.LI,J.XIAO,S.HE,J.WANG,Y.XU                       
REVDAT   3   04-FEB-15 4U7T    1       JRNL                                     
REVDAT   2   17-DEC-14 4U7T    1       JRNL                                     
REVDAT   1   12-NOV-14 4U7T    0                                                
JRNL        AUTH   X.GUO,L.WANG,J.LI,Z.DING,J.XIAO,X.YIN,S.HE,P.SHI,L.DONG,     
JRNL        AUTH 2 G.LI,C.TIAN,J.WANG,Y.CONG,Y.XU                               
JRNL        TITL   STRUCTURAL INSIGHT INTO AUTOINHIBITION AND HISTONE           
JRNL        TITL 2 H3-INDUCED ACTIVATION OF DNMT3A                              
JRNL        REF    NATURE                        V. 517   640 2015              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   25383530                                                     
JRNL        DOI    10.1038/NATURE13899                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.21                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 52407                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2667                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 40.2173 -  7.7187    0.98     2627   157  0.1951 0.2180        
REMARK   3     2  7.7187 -  6.1336    1.00     2628   152  0.2109 0.2598        
REMARK   3     3  6.1336 -  5.3603    1.00     2639   150  0.2078 0.2642        
REMARK   3     4  5.3603 -  4.8711    1.00     2652   123  0.1851 0.1829        
REMARK   3     5  4.8711 -  4.5225    1.00     2639   131  0.1720 0.2228        
REMARK   3     6  4.5225 -  4.2562    1.00     2614   143  0.1784 0.2071        
REMARK   3     7  4.2562 -  4.0432    1.00     2627   155  0.2034 0.2106        
REMARK   3     8  4.0432 -  3.8674    1.00     2614   131  0.2134 0.2743        
REMARK   3     9  3.8674 -  3.7186    1.00     2621   149  0.2439 0.3084        
REMARK   3    10  3.7186 -  3.5904    1.00     2589   156  0.2418 0.2763        
REMARK   3    11  3.5904 -  3.4782    1.00     2638   144  0.2639 0.3127        
REMARK   3    12  3.4782 -  3.3788    1.00     2611   131  0.2637 0.3272        
REMARK   3    13  3.3788 -  3.2899    1.00     2610   137  0.3025 0.3229        
REMARK   3    14  3.2899 -  3.2096    1.00     2626   130  0.2828 0.3297        
REMARK   3    15  3.2096 -  3.1367    1.00     2637   127  0.2910 0.4118        
REMARK   3    16  3.1367 -  3.0700    1.00     2577   137  0.3017 0.3574        
REMARK   3    17  3.0700 -  3.0086    1.00     2654   119  0.3298 0.3904        
REMARK   3    18  3.0086 -  2.9518    1.00     2589   156  0.3207 0.3977        
REMARK   3    19  2.9518 -  2.8991    0.97     2548   139  0.3695 0.4063        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.460            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.490           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 77.28                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 83.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010          10286                                  
REMARK   3   ANGLE     :  1.408          13910                                  
REMARK   3   CHIRALITY :  0.056           1480                                  
REMARK   3   PLANARITY :  0.006           1792                                  
REMARK   3   DIHEDRAL  : 17.287           3846                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 3                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 3913                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 2                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN B                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 1674                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3   NCS GROUP : 3                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN F                                     
REMARK   3     SELECTION          : CHAIN G                                     
REMARK   3     ATOM PAIRS NUMBER  : 80                                          
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4U7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202955.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.3-5.6                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52477                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.900                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 139.3000                           
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3A1A, 2QRV                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM ACETATE, 0.6M AMMONIUM       
REMARK 280  SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.17667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       41.08833            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       61.63250            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       20.54417            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      102.72083            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, F, G                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   468                                                      
REMARK 465     PRO A   469                                                      
REMARK 465     LEU A   470                                                      
REMARK 465     GLY A   471                                                      
REMARK 465     SER A   472                                                      
REMARK 465     PRO A   473                                                      
REMARK 465     ASN A   611                                                      
REMARK 465     ASN A   612                                                      
REMARK 465     HIS A   613                                                      
REMARK 465     ASP A   614                                                      
REMARK 465     GLN A   615                                                      
REMARK 465     GLU A   616                                                      
REMARK 465     PHE A   617                                                      
REMARK 465     ASP A   618                                                      
REMARK 465     PRO A   619                                                      
REMARK 465     PRO A   620                                                      
REMARK 465     THR A   834                                                      
REMARK 465     THR A   835                                                      
REMARK 465     ARG A   836                                                      
REMARK 465     SER A   837                                                      
REMARK 465     ASN A   838                                                      
REMARK 465     SER A   839                                                      
REMARK 465     ILE A   840                                                      
REMARK 465     LYS A   841                                                      
REMARK 465     GLN A   842                                                      
REMARK 465     GLY A   843                                                      
REMARK 465     LYS A   844                                                      
REMARK 465     ASP A   845                                                      
REMARK 465     GLY B   171                                                      
REMARK 465     PRO B   172                                                      
REMARK 465     LEU B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     SER B   175                                                      
REMARK 465     GLU B   176                                                      
REMARK 465     SER B   316                                                      
REMARK 465     LEU B   317                                                      
REMARK 465     GLN B   318                                                      
REMARK 465     ASN B   319                                                      
REMARK 465     ALA B   320                                                      
REMARK 465     ARG B   333                                                      
REMARK 465     HIS B   334                                                      
REMARK 465     TRP B   335                                                      
REMARK 465     GLN B   351                                                      
REMARK 465     LYS B   354                                                      
REMARK 465     LEU B   355                                                      
REMARK 465     ALA B   356                                                      
REMARK 465     ALA B   357                                                      
REMARK 465     LYS B   358                                                      
REMARK 465     TRP B   359                                                      
REMARK 465     PRO B   360                                                      
REMARK 465     GLY C   468                                                      
REMARK 465     PRO C   469                                                      
REMARK 465     LEU C   470                                                      
REMARK 465     GLY C   471                                                      
REMARK 465     SER C   472                                                      
REMARK 465     PRO C   473                                                      
REMARK 465     ASN C   611                                                      
REMARK 465     ASN C   612                                                      
REMARK 465     HIS C   613                                                      
REMARK 465     ASP C   614                                                      
REMARK 465     GLN C   615                                                      
REMARK 465     GLU C   616                                                      
REMARK 465     PHE C   617                                                      
REMARK 465     ASP C   618                                                      
REMARK 465     PRO C   619                                                      
REMARK 465     THR C   834                                                      
REMARK 465     THR C   835                                                      
REMARK 465     ARG C   836                                                      
REMARK 465     SER C   837                                                      
REMARK 465     ASN C   838                                                      
REMARK 465     SER C   839                                                      
REMARK 465     ILE C   840                                                      
REMARK 465     LYS C   841                                                      
REMARK 465     GLN C   842                                                      
REMARK 465     GLY C   843                                                      
REMARK 465     LYS C   844                                                      
REMARK 465     ASP C   845                                                      
REMARK 465     GLY D   171                                                      
REMARK 465     PRO D   172                                                      
REMARK 465     LEU D   173                                                      
REMARK 465     GLY D   174                                                      
REMARK 465     SER D   175                                                      
REMARK 465     GLU D   176                                                      
REMARK 465     GLY D   314                                                      
REMARK 465     GLY D   315                                                      
REMARK 465     SER D   316                                                      
REMARK 465     LEU D   317                                                      
REMARK 465     GLN D   318                                                      
REMARK 465     ASN D   319                                                      
REMARK 465     LYS D   354                                                      
REMARK 465     LEU D   355                                                      
REMARK 465     ALA D   356                                                      
REMARK 465     ALA D   357                                                      
REMARK 465     LYS D   358                                                      
REMARK 465     TRP D   359                                                      
REMARK 465     THR F    11                                                      
REMARK 465     GLY F    12                                                      
REMARK 465     THR G    11                                                      
REMARK 465     GLY G    12                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    THR D   245     ND2  ASN D   287              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS B   230     OE1  GLU D   180     2664     2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 849   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    PRO C 904   C   -  N   -  CA  ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    PRO D 310   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 501       49.62    -73.25                                   
REMARK 500    THR A 503      -54.32   -122.64                                   
REMARK 500    TYR A 526       35.21    -91.95                                   
REMARK 500    ILE A 539      -71.77    -79.40                                   
REMARK 500    ASN A 553       -9.43     71.62                                   
REMARK 500    LEU A 565      -67.00   -125.39                                   
REMARK 500    TYR A 592       55.72   -145.77                                   
REMARK 500    ASP A 686      135.79    -38.89                                   
REMARK 500    ALA A 760       42.95    -71.68                                   
REMARK 500    VAL A 785       -4.31   -143.58                                   
REMARK 500    GLU A 814      117.34     79.12                                   
REMARK 500    GLU A 854      -14.76     62.29                                   
REMARK 500    HIS A 873        9.83     85.52                                   
REMARK 500    VAL A 877      -51.49   -135.69                                   
REMARK 500    SER A 878     -144.99   -111.18                                   
REMARK 500    PHE B 196      -59.48   -122.54                                   
REMARK 500    PHE B 196      -58.11   -122.54                                   
REMARK 500    GLU B 202      -15.27   -158.75                                   
REMARK 500    VAL B 222      -58.76   -136.40                                   
REMARK 500    THR B 225      -46.34    -22.72                                   
REMARK 500    TRP B 235       29.84    -72.91                                   
REMARK 500    HIS B 250      -70.02    -63.98                                   
REMARK 500    THR B 251       68.42   -103.76                                   
REMARK 500    CYS B 252       70.43   -118.82                                   
REMARK 500    HIS B 313      -58.78   -158.42                                   
REMARK 500    ASN C 501       48.96    -72.76                                   
REMARK 500    THR C 503      -53.37   -122.43                                   
REMARK 500    TYR C 526       34.35    -92.03                                   
REMARK 500    ILE C 539      -70.72    -79.33                                   
REMARK 500    ASN C 553       -9.67     72.02                                   
REMARK 500    LEU C 565      -66.81   -124.42                                   
REMARK 500    TYR C 592       52.74   -149.02                                   
REMARK 500    GLN C 678       42.32     70.51                                   
REMARK 500    ARG C 720      137.70    -35.73                                   
REMARK 500    ALA C 760       44.41    -73.61                                   
REMARK 500    VAL C 785       -4.18   -143.96                                   
REMARK 500    GLU C 814      117.74     78.34                                   
REMARK 500    GLU C 854      -11.91     62.68                                   
REMARK 500    HIS C 873        9.26     87.17                                   
REMARK 500    VAL C 877      -50.93   -135.17                                   
REMARK 500    SER C 878     -145.13   -111.67                                   
REMARK 500    PHE D 196      -56.37   -123.31                                   
REMARK 500    LYS D 201      -80.60    -46.87                                   
REMARK 500    VAL D 222      -58.98   -135.21                                   
REMARK 500    THR D 225      -44.44    -25.60                                   
REMARK 500    TRP D 235       28.40    -72.66                                   
REMARK 500    HIS D 250      -71.98    -61.85                                   
REMARK 500    THR D 251       69.70   -106.37                                   
REMARK 500    CYS D 252       68.17   -116.86                                   
REMARK 500    ASP D 311     -126.37    -91.60                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS B  201     GLU B  202                  148.00                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 494   SG                                                     
REMARK 620 2 CYS A 497   SG  121.4                                              
REMARK 620 3 CYS A 514   SG  119.4 101.4                                        
REMARK 620 4 CYS A 517   SG  118.2  97.8  93.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 537   SG                                                     
REMARK 620 2 CYS A 540   SG   96.7                                              
REMARK 620 3 CYS A 559   SG  115.8 113.9                                        
REMARK 620 4 CYS A 562   SG  101.6 115.3 112.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 549   SG                                                     
REMARK 620 2 CYS A 554   SG   95.8                                              
REMARK 620 3 CYS A 583   SG   99.4 125.2                                        
REMARK 620 4 CYS A 586   SG  123.8 107.5 106.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 494   SG                                                     
REMARK 620 2 CYS C 497   SG  124.3                                              
REMARK 620 3 CYS C 514   SG  115.3  98.8                                        
REMARK 620 4 CYS C 517   SG  119.4  97.0  96.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 537   SG                                                     
REMARK 620 2 CYS C 540   SG   95.3                                              
REMARK 620 3 CYS C 559   SG  112.1 102.8                                        
REMARK 620 4 CYS C 562   SG  110.2 121.6 113.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 549   SG                                                     
REMARK 620 2 CYS C 554   SG   93.0                                              
REMARK 620 3 CYS C 583   SG   96.5 123.8                                        
REMARK 620 4 CYS C 586   SG  127.4 109.4 107.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH C 1004                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4U7P   RELATED DB: PDB                                   
DBREF  4U7T A  476   912  UNP    Q9Y6K1   DNM3A_HUMAN    476    912             
DBREF  4U7T B  178   379  UNP    Q9UJW3   DNM3L_HUMAN    178    379             
DBREF  4U7T C  476   912  UNP    Q9Y6K1   DNM3A_HUMAN    476    912             
DBREF  4U7T D  178   379  UNP    Q9UJW3   DNM3L_HUMAN    178    379             
DBREF  4U7T F    1    12  UNP    P84243   H33_HUMAN        2     13             
DBREF  4U7T G    1    12  UNP    P84243   H33_HUMAN        2     13             
SEQADV 4U7T GLY A  468  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T PRO A  469  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T LEU A  470  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T GLY A  471  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T SER A  472  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T PRO A  473  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T GLU A  474  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T PHE A  475  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T GLY B  171  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T PRO B  172  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T LEU B  173  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T GLY B  174  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T SER B  175  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T GLU B  176  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T PHE B  177  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T GLY C  468  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T PRO C  469  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T LEU C  470  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T GLY C  471  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T SER C  472  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T PRO C  473  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T GLU C  474  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T PHE C  475  UNP  Q9Y6K1              EXPRESSION TAG                 
SEQADV 4U7T GLY D  171  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T PRO D  172  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T LEU D  173  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T GLY D  174  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T SER D  175  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T GLU D  176  UNP  Q9UJW3              EXPRESSION TAG                 
SEQADV 4U7T PHE D  177  UNP  Q9UJW3              EXPRESSION TAG                 
SEQRES   1 A  445  GLY PRO LEU GLY SER PRO GLU PHE ARG GLU ARG LEU VAL          
SEQRES   2 A  445  TYR GLU VAL ARG GLN LYS CYS ARG ASN ILE GLU ASP ILE          
SEQRES   3 A  445  CYS ILE SER CYS GLY SER LEU ASN VAL THR LEU GLU HIS          
SEQRES   4 A  445  PRO LEU PHE VAL GLY GLY MET CYS GLN ASN CYS LYS ASN          
SEQRES   5 A  445  CYS PHE LEU GLU CYS ALA TYR GLN TYR ASP ASP ASP GLY          
SEQRES   6 A  445  TYR GLN SER TYR CYS THR ILE CYS CYS GLY GLY ARG GLU          
SEQRES   7 A  445  VAL LEU MET CYS GLY ASN ASN ASN CYS CYS ARG CYS PHE          
SEQRES   8 A  445  CYS VAL GLU CYS VAL ASP LEU LEU VAL GLY PRO GLY ALA          
SEQRES   9 A  445  ALA GLN ALA ALA ILE LYS GLU ASP PRO TRP ASN CYS TYR          
SEQRES  10 A  445  MET CYS GLY HIS LYS GLY THR TYR GLY LEU LEU ARG ARG          
SEQRES  11 A  445  ARG GLU ASP TRP PRO SER ARG LEU GLN MET PHE PHE ALA          
SEQRES  12 A  445  ASN ASN HIS ASP GLN GLU PHE ASP PRO PRO LYS VAL TYR          
SEQRES  13 A  445  PRO PRO VAL PRO ALA GLU LYS ARG LYS PRO ILE ARG VAL          
SEQRES  14 A  445  LEU SER LEU PHE ASP GLY ILE ALA THR GLY LEU LEU VAL          
SEQRES  15 A  445  LEU LYS ASP LEU GLY ILE GLN VAL ASP ARG TYR ILE ALA          
SEQRES  16 A  445  SER GLU VAL CYS GLU ASP SER ILE THR VAL GLY MET VAL          
SEQRES  17 A  445  ARG HIS GLN GLY LYS ILE MET TYR VAL GLY ASP VAL ARG          
SEQRES  18 A  445  SER VAL THR GLN LYS HIS ILE GLN GLU TRP GLY PRO PHE          
SEQRES  19 A  445  ASP LEU VAL ILE GLY GLY SER PRO CYS ASN ASP LEU SER          
SEQRES  20 A  445  ILE VAL ASN PRO ALA ARG LYS GLY LEU TYR GLU GLY THR          
SEQRES  21 A  445  GLY ARG LEU PHE PHE GLU PHE TYR ARG LEU LEU HIS ASP          
SEQRES  22 A  445  ALA ARG PRO LYS GLU GLY ASP ASP ARG PRO PHE PHE TRP          
SEQRES  23 A  445  LEU PHE GLU ASN VAL VAL ALA MET GLY VAL SER ASP LYS          
SEQRES  24 A  445  ARG ASP ILE SER ARG PHE LEU GLU SER ASN PRO VAL MET          
SEQRES  25 A  445  ILE ASP ALA LYS GLU VAL SER ALA ALA HIS ARG ALA ARG          
SEQRES  26 A  445  TYR PHE TRP GLY ASN LEU PRO GLY MET ASN ARG PRO LEU          
SEQRES  27 A  445  ALA SER THR VAL ASN ASP LYS LEU GLU LEU GLN GLU CYS          
SEQRES  28 A  445  LEU GLU HIS GLY ARG ILE ALA LYS PHE SER LYS VAL ARG          
SEQRES  29 A  445  THR ILE THR THR ARG SER ASN SER ILE LYS GLN GLY LYS          
SEQRES  30 A  445  ASP GLN HIS PHE PRO VAL PHE MET ASN GLU LYS GLU ASP          
SEQRES  31 A  445  ILE LEU TRP CYS THR GLU MET GLU ARG VAL PHE GLY PHE          
SEQRES  32 A  445  PRO VAL HIS TYR THR ASP VAL SER ASN MET SER ARG LEU          
SEQRES  33 A  445  ALA ARG GLN ARG LEU LEU GLY ARG SER TRP SER VAL PRO          
SEQRES  34 A  445  VAL ILE ARG HIS LEU PHE ALA PRO LEU LYS GLU TYR PHE          
SEQRES  35 A  445  ALA CYS VAL                                                  
SEQRES   1 B  209  GLY PRO LEU GLY SER GLU PHE MET PHE GLU THR VAL PRO          
SEQRES   2 B  209  VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU PHE          
SEQRES   3 B  209  GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE LEU          
SEQRES   4 B  209  GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL VAL          
SEQRES   5 B  209  ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU TRP          
SEQRES   6 B  209  GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO LEU          
SEQRES   7 B  209  GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU PHE          
SEQRES   8 B  209  GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS PRO          
SEQRES   9 B  209  GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP ASN          
SEQRES  10 B  209  LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER ARG          
SEQRES  11 B  209  PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL HIS          
SEQRES  12 B  209  GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER ASN          
SEQRES  13 B  209  ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL SER          
SEQRES  14 B  209  GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN SER          
SEQRES  15 B  209  SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL LYS          
SEQRES  16 B  209  ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR PHE          
SEQRES  17 B  209  SER                                                          
SEQRES   1 C  445  GLY PRO LEU GLY SER PRO GLU PHE ARG GLU ARG LEU VAL          
SEQRES   2 C  445  TYR GLU VAL ARG GLN LYS CYS ARG ASN ILE GLU ASP ILE          
SEQRES   3 C  445  CYS ILE SER CYS GLY SER LEU ASN VAL THR LEU GLU HIS          
SEQRES   4 C  445  PRO LEU PHE VAL GLY GLY MET CYS GLN ASN CYS LYS ASN          
SEQRES   5 C  445  CYS PHE LEU GLU CYS ALA TYR GLN TYR ASP ASP ASP GLY          
SEQRES   6 C  445  TYR GLN SER TYR CYS THR ILE CYS CYS GLY GLY ARG GLU          
SEQRES   7 C  445  VAL LEU MET CYS GLY ASN ASN ASN CYS CYS ARG CYS PHE          
SEQRES   8 C  445  CYS VAL GLU CYS VAL ASP LEU LEU VAL GLY PRO GLY ALA          
SEQRES   9 C  445  ALA GLN ALA ALA ILE LYS GLU ASP PRO TRP ASN CYS TYR          
SEQRES  10 C  445  MET CYS GLY HIS LYS GLY THR TYR GLY LEU LEU ARG ARG          
SEQRES  11 C  445  ARG GLU ASP TRP PRO SER ARG LEU GLN MET PHE PHE ALA          
SEQRES  12 C  445  ASN ASN HIS ASP GLN GLU PHE ASP PRO PRO LYS VAL TYR          
SEQRES  13 C  445  PRO PRO VAL PRO ALA GLU LYS ARG LYS PRO ILE ARG VAL          
SEQRES  14 C  445  LEU SER LEU PHE ASP GLY ILE ALA THR GLY LEU LEU VAL          
SEQRES  15 C  445  LEU LYS ASP LEU GLY ILE GLN VAL ASP ARG TYR ILE ALA          
SEQRES  16 C  445  SER GLU VAL CYS GLU ASP SER ILE THR VAL GLY MET VAL          
SEQRES  17 C  445  ARG HIS GLN GLY LYS ILE MET TYR VAL GLY ASP VAL ARG          
SEQRES  18 C  445  SER VAL THR GLN LYS HIS ILE GLN GLU TRP GLY PRO PHE          
SEQRES  19 C  445  ASP LEU VAL ILE GLY GLY SER PRO CYS ASN ASP LEU SER          
SEQRES  20 C  445  ILE VAL ASN PRO ALA ARG LYS GLY LEU TYR GLU GLY THR          
SEQRES  21 C  445  GLY ARG LEU PHE PHE GLU PHE TYR ARG LEU LEU HIS ASP          
SEQRES  22 C  445  ALA ARG PRO LYS GLU GLY ASP ASP ARG PRO PHE PHE TRP          
SEQRES  23 C  445  LEU PHE GLU ASN VAL VAL ALA MET GLY VAL SER ASP LYS          
SEQRES  24 C  445  ARG ASP ILE SER ARG PHE LEU GLU SER ASN PRO VAL MET          
SEQRES  25 C  445  ILE ASP ALA LYS GLU VAL SER ALA ALA HIS ARG ALA ARG          
SEQRES  26 C  445  TYR PHE TRP GLY ASN LEU PRO GLY MET ASN ARG PRO LEU          
SEQRES  27 C  445  ALA SER THR VAL ASN ASP LYS LEU GLU LEU GLN GLU CYS          
SEQRES  28 C  445  LEU GLU HIS GLY ARG ILE ALA LYS PHE SER LYS VAL ARG          
SEQRES  29 C  445  THR ILE THR THR ARG SER ASN SER ILE LYS GLN GLY LYS          
SEQRES  30 C  445  ASP GLN HIS PHE PRO VAL PHE MET ASN GLU LYS GLU ASP          
SEQRES  31 C  445  ILE LEU TRP CYS THR GLU MET GLU ARG VAL PHE GLY PHE          
SEQRES  32 C  445  PRO VAL HIS TYR THR ASP VAL SER ASN MET SER ARG LEU          
SEQRES  33 C  445  ALA ARG GLN ARG LEU LEU GLY ARG SER TRP SER VAL PRO          
SEQRES  34 C  445  VAL ILE ARG HIS LEU PHE ALA PRO LEU LYS GLU TYR PHE          
SEQRES  35 C  445  ALA CYS VAL                                                  
SEQRES   1 D  209  GLY PRO LEU GLY SER GLU PHE MET PHE GLU THR VAL PRO          
SEQRES   2 D  209  VAL TRP ARG ARG GLN PRO VAL ARG VAL LEU SER LEU PHE          
SEQRES   3 D  209  GLU ASP ILE LYS LYS GLU LEU THR SER LEU GLY PHE LEU          
SEQRES   4 D  209  GLU SER GLY SER ASP PRO GLY GLN LEU LYS HIS VAL VAL          
SEQRES   5 D  209  ASP VAL THR ASP THR VAL ARG LYS ASP VAL GLU GLU TRP          
SEQRES   6 D  209  GLY PRO PHE ASP LEU VAL TYR GLY ALA THR PRO PRO LEU          
SEQRES   7 D  209  GLY HIS THR CYS ASP ARG PRO PRO SER TRP TYR LEU PHE          
SEQRES   8 D  209  GLN PHE HIS ARG LEU LEU GLN TYR ALA ARG PRO LYS PRO          
SEQRES   9 D  209  GLY SER PRO ARG PRO PHE PHE TRP MET PHE VAL ASP ASN          
SEQRES  10 D  209  LEU VAL LEU ASN LYS GLU ASP LEU ASP VAL ALA SER ARG          
SEQRES  11 D  209  PHE LEU GLU MET GLU PRO VAL THR ILE PRO ASP VAL HIS          
SEQRES  12 D  209  GLY GLY SER LEU GLN ASN ALA VAL ARG VAL TRP SER ASN          
SEQRES  13 D  209  ILE PRO ALA ILE ARG SER ARG HIS TRP ALA LEU VAL SER          
SEQRES  14 D  209  GLU GLU GLU LEU SER LEU LEU ALA GLN ASN LYS GLN SER          
SEQRES  15 D  209  SER LYS LEU ALA ALA LYS TRP PRO THR LYS LEU VAL LYS          
SEQRES  16 D  209  ASN CYS PHE LEU PRO LEU ARG GLU TYR PHE LYS TYR PHE          
SEQRES  17 D  209  SER                                                          
SEQRES   1 F   12  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY              
SEQRES   1 G   12  ALA ARG THR LYS GLN THR ALA ARG LYS SER THR GLY              
HET     ZN  A1001       1                                                       
HET     ZN  A1002       1                                                       
HET     ZN  A1003       1                                                       
HET    SAH  A1004      26                                                       
HET     ZN  C1001       1                                                       
HET     ZN  C1002       1                                                       
HET     ZN  C1003       1                                                       
HET    SAH  C1004      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   7   ZN    6(ZN 2+)                                                     
FORMUL  10  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL  15  HOH   *11(H2 O)                                                     
HELIX    1 AA1 ARG A  476  GLN A  485  1                                  10    
HELIX    2 AA2 ASN A  489  ILE A  493  5                                   5    
HELIX    3 AA3 CYS A  514  ALA A  525  1                                  12    
HELIX    4 AA4 VAL A  560  VAL A  567  1                                   8    
HELIX    5 AA5 GLY A  570  GLU A  578  1                                   9    
HELIX    6 AA6 ASP A  600  PHE A  609  1                                  10    
HELIX    7 AA7 PRO A  627  ARG A  631  5                                   5    
HELIX    8 AA8 ALA A  644  GLY A  654  1                                  11    
HELIX    9 AA9 CYS A  666  GLN A  678  1                                  13    
HELIX   10 AB1 ASP A  686  VAL A  690  5                                   5    
HELIX   11 AB2 THR A  691  TRP A  698  1                                   8    
HELIX   12 AB3 ARG A  729  ARG A  742  1                                  14    
HELIX   13 AB4 GLY A  762  LEU A  773  1                                  12    
HELIX   14 AB5 LYS A  783  VAL A  785  5                                   3    
HELIX   15 AB6 GLU A  814  LEU A  819  5                                   6    
HELIX   16 AB7 TRP A  860  PHE A  868  1                                   9    
HELIX   17 AB8 SER A  881  SER A  892  1                                  12    
HELIX   18 AB9 SER A  894  ALA A  903  1                                  10    
HELIX   19 AC1 PRO A  904  TYR A  908  5                                   5    
HELIX   20 AC2 PRO B  183  ARG B  187  5                                   5    
HELIX   21 AC3 ILE B  199  THR B  204  1                                   6    
HELIX   22 AC4 ASP B  223  THR B  227  5                                   5    
HELIX   23 AC5 VAL B  228  TRP B  235  1                                   8    
HELIX   24 AC6 PRO B  255  ARG B  271  1                                  17    
HELIX   25 AC7 ASN B  291  LEU B  302  1                                  12    
HELIX   26 AC8 SER B  339  LYS B  350  1                                  12    
HELIX   27 AC9 VAL B  364  TYR B  374  5                                  11    
HELIX   28 AD1 ARG C  476  GLN C  485  1                                  10    
HELIX   29 AD2 ASN C  489  ILE C  493  5                                   5    
HELIX   30 AD3 CYS C  514  ALA C  525  1                                  12    
HELIX   31 AD4 VAL C  560  VAL C  567  1                                   8    
HELIX   32 AD5 GLY C  570  GLU C  578  1                                   9    
HELIX   33 AD6 ASP C  600  PHE C  609  1                                  10    
HELIX   34 AD7 ALA C  644  LEU C  653  1                                  10    
HELIX   35 AD8 CYS C  666  GLN C  678  1                                  13    
HELIX   36 AD9 ASP C  686  VAL C  690  5                                   5    
HELIX   37 AE1 THR C  691  TRP C  698  1                                   8    
HELIX   38 AE2 ARG C  729  ARG C  742  1                                  14    
HELIX   39 AE3 GLY C  762  LEU C  773  1                                  12    
HELIX   40 AE4 LYS C  783  VAL C  785  5                                   3    
HELIX   41 AE5 GLU C  814  LEU C  819  5                                   6    
HELIX   42 AE6 TRP C  860  PHE C  868  1                                   9    
HELIX   43 AE7 SER C  881  SER C  892  1                                  12    
HELIX   44 AE8 SER C  894  ALA C  903  1                                  10    
HELIX   45 AE9 PRO C  904  TYR C  908  5                                   5    
HELIX   46 AF1 PRO D  183  ARG D  187  5                                   5    
HELIX   47 AF2 ILE D  199  LEU D  206  1                                   8    
HELIX   48 AF3 ASP D  223  THR D  227  5                                   5    
HELIX   49 AF4 VAL D  228  TRP D  235  1                                   8    
HELIX   50 AF5 PRO D  255  ARG D  271  1                                  17    
HELIX   51 AF6 ASN D  291  LEU D  302  1                                  12    
HELIX   52 AF7 ALA D  329  ARG D  333  5                                   5    
HELIX   53 AF8 SER D  339  LYS D  350  1                                  12    
HELIX   54 AF9 VAL D  364  TYR D  374  5                                  11    
SHEET    1 AA1 2 LEU A 504  GLU A 505  0                                        
SHEET    2 AA1 2 GLY A 512  MET A 513 -1  O  MET A 513   N  LEU A 504           
SHEET    1 AA2 3 CYS A 557  CYS A 559  0                                        
SHEET    2 AA2 3 GLU A 545  MET A 548 -1  N  LEU A 547   O  PHE A 558           
SHEET    3 AA2 3 THR F   3  GLN F   5 -1  O  LYS F   4   N  VAL A 546           
SHEET    1 AA3 7 MET A 682  VAL A 684  0                                        
SHEET    2 AA3 7 VAL A 657  SER A 663  1  N  ALA A 662   O  MET A 682           
SHEET    3 AA3 7 ILE A 634  LEU A 639  1  N  VAL A 636   O  ILE A 661           
SHEET    4 AA3 7 LEU A 703  GLY A 706  1  O  LEU A 703   N  LEU A 637           
SHEET    5 AA3 7 PHE A 752  VAL A 758  1  O  PHE A 752   N  VAL A 704           
SHEET    6 AA3 7 ALA A 791  GLY A 796 -1  O  TRP A 795   N  PHE A 755           
SHEET    7 AA3 7 VAL A 778  ASP A 781 -1  N  ILE A 780   O  ARG A 792           
SHEET    1 AA4 2 ALA A 788  HIS A 789  0                                        
SHEET    2 AA4 2 VAL A 830  ARG A 831  1  O  VAL A 830   N  HIS A 789           
SHEET    1 AA5 3 ARG A 823  ALA A 825  0                                        
SHEET    2 AA5 3 VAL A 850  MET A 852 -1  O  PHE A 851   N  ILE A 824           
SHEET    3 AA5 3 LYS A 855  ASP A 857 -1  O  LYS A 855   N  MET A 852           
SHEET    1 AA6 6 LEU B 218  HIS B 220  0                                        
SHEET    2 AA6 6 VAL B 192  SER B 194  1  N  SER B 194   O  LYS B 219           
SHEET    3 AA6 6 LEU B 240  ALA B 244  1  O  TYR B 242   N  LEU B 193           
SHEET    4 AA6 6 PHE B 281  ASP B 286  1  O  MET B 283   N  VAL B 241           
SHEET    5 AA6 6 ARG B 322  SER B 325 -1  O  ARG B 322   N  ASP B 286           
SHEET    6 AA6 6 VAL B 307  THR B 308 -1  N  VAL B 307   O  VAL B 323           
SHEET    1 AA7 2 LEU C 504  GLU C 505  0                                        
SHEET    2 AA7 2 GLY C 512  MET C 513 -1  O  MET C 513   N  LEU C 504           
SHEET    1 AA8 3 CYS C 557  CYS C 559  0                                        
SHEET    2 AA8 3 GLU C 545  MET C 548 -1  N  LEU C 547   O  PHE C 558           
SHEET    3 AA8 3 THR G   3  GLN G   5 -1  O  LYS G   4   N  VAL C 546           
SHEET    1 AA9 7 MET C 682  VAL C 684  0                                        
SHEET    2 AA9 7 VAL C 657  SER C 663  1  N  ALA C 662   O  MET C 682           
SHEET    3 AA9 7 ILE C 634  LEU C 639  1  N  VAL C 636   O  ILE C 661           
SHEET    4 AA9 7 LEU C 703  GLY C 706  1  O  ILE C 705   N  LEU C 639           
SHEET    5 AA9 7 PHE C 752  VAL C 758  1  O  PHE C 752   N  VAL C 704           
SHEET    6 AA9 7 ALA C 791  GLY C 796 -1  O  TRP C 795   N  PHE C 755           
SHEET    7 AA9 7 VAL C 778  ASP C 781 -1  N  ILE C 780   O  ARG C 792           
SHEET    1 AB1 2 ALA C 788  HIS C 789  0                                        
SHEET    2 AB1 2 VAL C 830  ARG C 831  1  O  VAL C 830   N  HIS C 789           
SHEET    1 AB2 3 ARG C 823  ALA C 825  0                                        
SHEET    2 AB2 3 VAL C 850  MET C 852 -1  O  PHE C 851   N  ILE C 824           
SHEET    3 AB2 3 LYS C 855  ASP C 857 -1  O  LYS C 855   N  MET C 852           
SHEET    1 AB3 6 LEU D 218  HIS D 220  0                                        
SHEET    2 AB3 6 VAL D 192  SER D 194  1  N  SER D 194   O  LYS D 219           
SHEET    3 AB3 6 LEU D 240  ALA D 244  1  O  TYR D 242   N  LEU D 193           
SHEET    4 AB3 6 PHE D 281  ASP D 286  1  O  MET D 283   N  VAL D 241           
SHEET    5 AB3 6 VAL D 321  SER D 325 -1  O  TRP D 324   N  PHE D 284           
SHEET    6 AB3 6 VAL D 307  ILE D 309 -1  N  ILE D 309   O  VAL D 321           
LINK         SG  CYS A 494                ZN    ZN A1001     1555   1555  2.17  
LINK         SG  CYS A 497                ZN    ZN A1001     1555   1555  2.26  
LINK         SG  CYS A 514                ZN    ZN A1001     1555   1555  2.42  
LINK         SG  CYS A 517                ZN    ZN A1001     1555   1555  2.28  
LINK         SG  CYS A 537                ZN    ZN A1002     1555   1555  2.57  
LINK         SG  CYS A 540                ZN    ZN A1002     1555   1555  2.24  
LINK         SG  CYS A 549                ZN    ZN A1003     1555   1555  2.52  
LINK         SG  CYS A 554                ZN    ZN A1003     1555   1555  2.22  
LINK         SG  CYS A 559                ZN    ZN A1002     1555   1555  2.42  
LINK         SG  CYS A 562                ZN    ZN A1002     1555   1555  2.16  
LINK         SG  CYS A 583                ZN    ZN A1003     1555   1555  2.13  
LINK         SG  CYS A 586                ZN    ZN A1003     1555   1555  2.30  
LINK         SG  CYS C 494                ZN    ZN C1001     1555   1555  2.23  
LINK         SG  CYS C 497                ZN    ZN C1001     1555   1555  2.28  
LINK         SG  CYS C 514                ZN    ZN C1001     1555   1555  2.48  
LINK         SG  CYS C 517                ZN    ZN C1001     1555   1555  2.28  
LINK         SG  CYS C 537                ZN    ZN C1002     1555   1555  2.48  
LINK         SG  CYS C 540                ZN    ZN C1002     1555   1555  2.42  
LINK         SG  CYS C 549                ZN    ZN C1003     1555   1555  2.48  
LINK         SG  CYS C 554                ZN    ZN C1003     1555   1555  2.18  
LINK         SG  CYS C 559                ZN    ZN C1002     1555   1555  2.32  
LINK         SG  CYS C 562                ZN    ZN C1002     1555   1555  2.10  
LINK         SG  CYS C 583                ZN    ZN C1003     1555   1555  2.12  
LINK         SG  CYS C 586                ZN    ZN C1003     1555   1555  2.27  
CISPEP   1 PRO B  274    GLY B  275          0       -10.45                     
CISPEP   2 PRO D  274    GLY D  275          0       -11.02                     
CISPEP   3 PRO D  360    THR D  361          0         8.06                     
SITE     1 AC1  4 CYS A 494  CYS A 497  CYS A 514  CYS A 517                    
SITE     1 AC2  4 CYS A 537  CYS A 540  CYS A 559  CYS A 562                    
SITE     1 AC3  4 CYS A 549  CYS A 554  CYS A 583  CYS A 586                    
SITE     1 AC4 16 PHE A 640  ASP A 641  GLY A 642  ILE A 643                    
SITE     2 AC4 16 THR A 645  SER A 663  GLU A 664  VAL A 665                    
SITE     3 AC4 16 CYS A 666  ASP A 686  VAL A 687  ARG A 688                    
SITE     4 AC4 16 GLY A 707  ARG A 891  SER A 892  TRP A 893                    
SITE     1 AC5  4 CYS C 494  CYS C 497  CYS C 514  CYS C 517                    
SITE     1 AC6  4 CYS C 537  CYS C 540  CYS C 559  CYS C 562                    
SITE     1 AC7  4 CYS C 549  CYS C 554  CYS C 583  CYS C 586                    
SITE     1 AC8 17 PHE C 640  ASP C 641  GLY C 642  ILE C 643                    
SITE     2 AC8 17 THR C 645  SER C 663  GLU C 664  VAL C 665                    
SITE     3 AC8 17 CYS C 666  ASP C 686  VAL C 687  ARG C 688                    
SITE     4 AC8 17 GLY C 707  LEU C 730  ARG C 891  SER C 892                    
SITE     5 AC8 17 TRP C 893                                                     
CRYST1  183.823  183.823  123.265  90.00  90.00 120.00 P 65         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005440  0.003141  0.000000        0.00000                         
SCALE2      0.000000  0.006282  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008113        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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